A new time-resolved fluorescence spectrometer was designed to incorporate recent advances in laser technology. When completed, this facility will accurately determine very complex fluorescence decay kinetics arising from protein and membrane fluorophores. The rapid acquisition of lifetime data during transient (eg., stopped-flow) events is also tenable with this design. Specialized, powerful data analysis programs are needed to extract complex decay parameters from fluorescing systems. Thus new global analysis schemes were developed for this task. The combination of this state-of-the-art software with our new instrument should yield the highest level of information available from a fluorescence experiment. Preliminary studies of lifetime changes linked to protein conformational changes were conducted.